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经验公式(希尔记法):
C15H18N2O3S · C2HF3O2
化学文摘社编号:
分子量:
420.40
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352209
MDL number:
产品名称
L-Methionine 7-amido-4-methylcoumarin trifluoroacetate salt, ≥99.0% (sum of enantiomers, HPLC)
InChI key
VSAUWUJWXBUSEU-YDALLXLXSA-N
SMILES string
OC(=O)C(F)(F)F.CSCC[C@H](N)C(=O)Nc1ccc2C(C)=CC(=O)Oc2c1
InChI
1S/C15H18N2O3S.C2HF3O2/c1-9-7-14(18)20-13-8-10(3-4-11(9)13)17-15(19)12(16)5-6-21-2;3-2(4,5)1(6)7/h3-4,7-8,12H,5-6,16H2,1-2H3,(H,17,19);(H,6,7)/t12-;/m0./s1
assay
≥99.0% (sum of enantiomers, HPLC)
optical activity
[α]20/D +68±3°, c = 1% in methanol
storage temp.
2-8°C
Quality Level
Application
L-Methionine 7-amido-4-methylcoumarin trifluoroacetate and its analogues may be used to study the kinetics of methionine aminopeptidase (hMetAP2). L-Methionine 7-amido-4-methylcoumarin trifluoroacetate may be use with other substrates to assess the specificity of various aminopeptidases.
Other Notes
Substrate for calpain
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
Gabriel Rinaldi et al.
Molecular and biochemical parasitology, 167(2), 118-126 (2009-05-26)
Schistosoma mansoni leucine aminopeptidase (LAP) is thought to play a central role in hatching of the miracidium from the schistosome egg. We identified two discrete LAPs genes in the S. mansoni genome, and their orthologs in S. japonicum. The similarities
T Sasaki et al.
The Journal of biological chemistry, 259(20), 12489-12494 (1984-10-25)
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found to hydrolyze a variety of peptides and synthetic substrates. Leu-Trp-Met-Arg-Phe-Ala, eledoisin-related peptide, alpha-neoendorphin, angiotensin I, luteinizing hormone-releasing hormone, neurotensin, dynorphin, glucagon, and oxidized insulin B chain were cleaved with a general preference
G Yang et al.
Biochemistry, 40(35), 10645-10654 (2001-08-29)
The steady-state kinetics of a full-length and truncated form of the type 2 human methionine aminopeptidase (hMetAP2) were analyzed by continuous monitoring of the amide bond cleavage of various peptide substrates and methionyl analogues of 7-amido-4-methylcoumarin (AMC) and p-nitroaniline (pNA)
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